Myosin rod and light meromyosin (LMM) of walleye pollack and white croaker were examined for their rheological properties by measuring dynamic viscoelastic parameters. Rods from walleye pollack and white croaker increased their storage moduli (G') in the ranges of 29-43 degrees C and 31-38 degrees C, respectively, in temperature sweep analysis. Walleye pollack LMM showed no peak of G' upon heating, whereas the white croaker counterpart exhibited a single sharp peak of G' at 35 degrees C. Loss modulus (G") showed similar temperature-dependent changes for the two fish species as the case of G', irrespective of rod and LMM, although G" values were lower than those of G'. Thus, rheological properties of rod and LMM were different between walleye pollack and white croaker. Taken together with data previously reported for myosin, it was considered that both myosin rods from walleye pollack and white croaker are attributed to thermal gel formation of myosin in a low-temperature range, though in a species-specific manner.
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http://dx.doi.org/10.1021/jf051223h | DOI Listing |
J Sci Food Agric
January 2011
Department of Fisheries Technology, Bangladesh Agricultural University, Mymensingh 2202, Bangladesh.
Background: The physical attribute of heat-induced gel texture is highly dependent on the microstructure of the gel. In this study the microstructures of walleye pollack surimi gels preheated at various temperatures with and without inhibitors (ethylenediamine-N,N,N',N'-tetraacetic acid, iodoacetamide and leupeptin) were observed with a natural scanning electron microscope.
Results: Without inhibitors, gels preheated at 30 °C showed a fine and uniform network structure together with the highest polymerisation of myosin heavy chain (MHC) and the highest gel strength.
Pak J Biol Sci
January 2010
Laboratory of Aquatic Product Utilization, Faculty of Agriculture, Kochi University, Nankoku, Kochi 783-8502, Japan.
In order to clarify the effect of oxidation itself on the gel formation of salted-surimi through setting, the gel-forming properties were examined with or without transglutaminase (TGase) inhibitor. The gels were prepared from walleye pollack salted-surimi mixed with KBrO3 through setting at 30 degrees C (suwari gel) for 2 h prior to heating at 80 degrees C for 20 min (kamaboko gel) in the presence or absence of TGase inhibitor. The gel strength of kamaboko gel increased through setting but KBrO3 almost did not promote the gel formation of kamaboko gels through setting comparing with control.
View Article and Find Full Text PDFJ Agric Food Chem
November 2005
Laboratory of Aquatic Molecular Biology and Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo, Tokyo 113-8657, Japan.
Myosin rod and light meromyosin (LMM) of walleye pollack and white croaker were examined for their rheological properties by measuring dynamic viscoelastic parameters. Rods from walleye pollack and white croaker increased their storage moduli (G') in the ranges of 29-43 degrees C and 31-38 degrees C, respectively, in temperature sweep analysis. Walleye pollack LMM showed no peak of G' upon heating, whereas the white croaker counterpart exhibited a single sharp peak of G' at 35 degrees C.
View Article and Find Full Text PDFJ Biol Chem
November 2003
Central Research Laboratory, Nippon Suisan Kaisha, Ltd., Kitanomachi, Hachioji, Tokyo 192-0906, Japan.
Trimethylamine-N-oxide (TMAO) is abundant in marine fish. Formaldehyde synthesis by TMAO demethylation during storage markedly deteriorates fish meat. In the present work, we cloned the extremely aspartic acid-rich proteins from skeletal muscle of a commercially important species, walleye pollack, in the course of molecular identification of trimethylamine-N-oxide demethylase (TMAOase).
View Article and Find Full Text PDFJ Agric Food Chem
July 2003
Laboratory of Aquatic Molecular Biology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo, Tokyo 113-8657, Japan.
Fast skeletal light meromyosins (LMMs) of white croaker and walleye pollack were prepared in our expression system using Escherichia coli and determined for their polymer-forming ability and thermodynamic properties by using sodium dodecyl sulfate polyacrylamide gel electrophoresis and differential scanning calorimetry (DSC), respectively. White croaker LMM formed dimer by heating at 80 degrees C and showed only a single peak at 32.1 degrees C of temperature transition in DSC.
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